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Chengdu Henghui Pharmaceutical Co., Ltd.(expird)

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Chengdu Henghui Pharmaceutical Co., Ltd.(expird)

Business Type:Lab/Research institutions

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Year Established:
2017
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Chengdu Henghui Pharmaceutical Co., Ltd.(expird)

Country: China (Mainland)

Business Type:Lab/Research institutions

UNC1215

CAS NO.1415800-43-9

  • Min.Order: 10 Milligram
  • Payment Terms:
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Product Details

Keywords

  • UNC1215
  • UNC-1215
  • Chengdu Henghui Pharm Tec Co. Ltd

Quick Details

  • ProName: UNC1215
  • CasNo: 1415800-43-9
  • Molecular Formula: C32H43N5O2
  • Appearance: off-white powder
  • Application: For laboratory use only- not intended ...
  • ProductionCapacity: Metric Ton/Day
  • Purity: ≥98%
  • Storage: roottemperature
  • LimitNum: 10 Milligram

Superiority

We are a CRO company, and our Research and Development team is consisted of PhDs and Masters in chemistry and pharmacy.

We are committed to protect our customer’s privacy with the highest level of ethical standard. Our dedicated team will follow up on every order and provide instant feedback on the status to our customer.

We stand behind our product by providing a complete QA report. The test data of customer order can be provided upon request.

We make our efforts to offer customer innovative, customized, high-quality service.

Our custom manufacturing encompasses everything from pharmaceutical intermediates to API.

Details

UNC1215 is a potent and selective chemical probe for the methyllysine (Kme) reading function of L3MBTL3 with Kd value of 120 nM. IC50 Value: 120 nM (Kd) [1] Target: L3MBTL3 In vitro: UNC1215 binds L3MBTL3 with a K(d) of 120 nM, competitively displacing mono- or dimethyllysine-containing peptides, and is greater than 50-fold more potent toward L3MBTL3 than other members of the MBT family while also demonstrating selectivity against more than 200 other reader domains examined. X-ray crystallography identified a unique 2:2 polyvalent mode of interaction between UNC1215 and L3MBTL3. In cells, UNC1215 is nontoxic and directly binds L3MBTL3 via the Kme-binding pocket of the MBT domains. UNC1215 increases the cellular mobility of GFP-L3MBTL3 fusion proteins, and point mutants that disrupt the Kme-binding function of GFP-L3MBTL3 phenocopy the effects of UNC1215 on localization

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